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Figure 3
Key subunit interfaces for structures of BbDHFR-TS. Top left, arginine side chains from the opposite TS subunit (yellow) directly bind the terminal dUMP phosphate in the active site of one protomer (violet). Top right, the linker region from one protomer (gray) fits into a hydrophobic groove created by DHFR from the opposite protomer (green). Bottom, binding surface between the DHFR (pink), TS (yellow) and linker (gray) regions of protomer B of apo BbDHFR-TS, with labels for hydrogen-bonding residues. All distances are measured in Å. These figures were created using PDB entries 3i3r , 3k2h and 3nrr with PyMOL (DeLano, 2002BB12).

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 67| Part 9| August 2011| Pages 1070-1077
doi:10.1107/S1744309111029009
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